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CLINICAL CHEMISTRY 2 > Enzymology > Flashcards

Enzymology Flashcards

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1
Q

study of Enzymes

A

ENZYMOLOGY

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2
Q

catalyzed reactions are specific and essential to physiologic functions like

A
  • hydration of CO2
  • nerve conduction
  • nutrient degradation
  • energy use
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3
Q

Enzymes that facilitate **coagulation **are specific to

A

PLASMA

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4
Q

Biological catalyst (enzyme) mostly inhibit

A

Homogenous catalysis

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5
Q

Catalytic site; water free cavity

A

Active site

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6
Q

Allosteric site may bind

A

regulator molecules

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7
Q

How do these molecules inhibit or enhance substrate binding?

A

conformational change is introduced in the active site

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8
Q

Reaction rate is reduced when

A

there is conformational change due to allosteric inhibitor, unable to bind to enzyme and prevents it from lowering the activation energy

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9
Q

Cofactor and coenzyme bind temporarily and permanently through?

A

T: ionic and hydrogen bond
P: strong covalent bond

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10
Q

alters the spatial configuration of an enzyme for proper substrate binding

A

COFACTOR OR COENZYME

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11
Q

____ IS A TYPE OF COFACTOR

A

COENZYME

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12
Q

____ are covalently bound and can be removed by ________ the enzyme

A

some cofactors, denaturing

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13
Q

thermostable and form the active site of enzyme

A

Cofactor

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14
Q

true or false: coenzyme can catalyze a reaction by itself

A

false; coenzyme cannot catalyze by itself but has to bind to apoenzyme

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15
Q

Holoenzyme

A

coenzyme + apoenzyme;
comple and active form of enzyme

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16
Q

protein part of the enzyme; inactive form

A

apoenzyme

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17
Q

Catalytic components of DNA polymerase enzyme

A

apoenzyme

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18
Q

multi-subunit complex of DNA polymerase

A

holoenzyme

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19
Q

true or false: catalytic activity of enzymes depends on the **integrity of the enzymes’ 3D structure **

A

true

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20
Q

factors that act as denaturing agents

A
  • temperature
  • pH
  • chemicals
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21
Q

denaturation disrupts the ___ bonds

A

hydrogen bonds (that stabilize the 3D structure)

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22
Q

Enzymes like polymerases resume their activity at temperatures higher than

A

90 degrees Celsius

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23
Q

causes the unfolding of the enzyme

A

extremes of pH

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24
Q

In extremes of pH, unfolding can lead to loss of structural integrity then

A

loss of function

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25
____ bonding: secondary structure ____ bonding: tertiary structure
hydrogen; covalent
26
EC-IUB
Enzyme Commission of the International Union of Biochemistry
27
EC-IUB adopted a classification in ___, and was revised in ____ & ____
1961, 1972, 1978
28
EC CLASS 4
Lyases
29
EC Class 2
Transferases
30
reduction
gain of electrons
31
EC class of Lactate Dehydrogenase
Oxidoreductase | Class 1
32
conversion of ethanol to acetaldehyde in liver
Alcohol dehydrogenase
33
EC of Creatine Kinase
Transferase
34
In CK, a phosphate group from ATP is transfered to the _ atom of creatine phosphate
nitrogen
35
End products of CK
ADP and creatine phosphate
36
Cleavage of bonds with the addition of H2O
Hydrolases
37
EC of esterases | ACP, ALP
Hydrolases
38
group elimination to form double bonds (product)
LYASES
39
In Aldolases, it cleaves the 6-carbon molecule (fructose-1,6-diphosphate) to produce 2 3-carbon compounds:
glyceraldehyde-3-phosphate and dihydroxyacetone phosphate
40
True or false: Isomeric reactions are reversible
true
41
responsible for the conversion of carbohydrate, glucose, to toher compounds
Glycolytic pathway
42
EC class of mutases
Isomerase
43
triacylglycerol acylhydrolase
lipase
44
1,4-a-D-glucan glucanohydrolase
Amylase
45
In activation energy, reactants possessing enough energy to overcome the enrgy barrier participate in
product formation
46
Enzyme ___ free energy required to activate the reaction
reduces
47
true of false: transition state of the ES complex has a **lower activation energy** than transition state of the substrate aloe
true
48
Who are the two people who hypothesized the role ofsubstrate cocnentration in the formation of ES complex in 1913?
Michaelis and Mentern
49
Substrate readily binds to free enzymes at ____ concentration
low
50
FIRST ORDER: reaction rate is directly proportional to the ___________ concentration
substrate
51
further increase in substrate concentration no longer accelerates reaction due to
saturated enzyme with the susbtrate (no enzyme left to react)
52
Maximum velocity is achieved when
substrate concentration is high enough to saturate all available enzymes
53
Km
specifically the substrate concentration (enzyme yields 1/2 of the possible Vmax) amount of susbtrate needed for a particular enzyme reaction
54
double reciprocal plot (yields a straight line)
Lineweaver-Burk plot
55
higher the enzyme level
faster the reaction
56
pH is carefully controlled at an optimal pH by
buffer solutions
57
low temperatures render enzymes
reversibly inactive
58
Common Activators (Inorganic Cofactors)
Metallic: Ca2+, Fe2+, Mg2+, Mn2+, Zn2+, K+ Non-metallic: Br-, Cl-
59
Common Coenzymes (Organic factors)
Nucleotide phosphates, Vitamins
60
true or false: Km is constant for each enzyme and **can be altered**
false: cannot be altered
61
presence of compettive inhibitors will ___ the maximum velocity
lower
62
bind to enzyme at a place other than the active site; metallic
noncompetitive inhibitors
63
true or false: both inhibitor and susbtrate bind to enzyme simultaneously
true
64
binds to the Enzyme-Substrate (ES) complex
Uncompetitive Inhibitors
65
example of antienzyme
Trypsin inhibitors
66
In rate of reaction, velocity constant o the reaction of the inhibitor with enzyme is
measure of the effectiveness of the inhibitor
67
convenient method of enzyme quantitation
measurement of enzyme activity (not directly the enzyme)
68
amount f susbtrate exceeds that of enzyme, rate of reaction will depend on the
ENZYME CONCENTRATION
69
Period for Analysis sequence
1. Enzyme is initially introduced 2. Excess substrate steadily combine with available enzyme 3. Reaction rate increases 4. Enzyme is saturated 5. Rate of product formation, release of enzyme, and recombination proceed linearly
70
In fixed time, reaction is stopped, by inactivating enzyme with
weak acid
71
also known as Kinetic Assays
Continuous-Monitoring
72
Causes of deviation from linearity
* enzyme is elevated: substrate is used up too early * coenzyme conc. is low
73
variables that may alter results
pH, temperature, substrate
74
Enzyme conc is usually expressed as
Units per Liter (IU/L)
75
alternativeof measurement of enzyme activity
measurement of enzyme mass
76
example of digestive enzyme where inactive precursors and inhibtors of catalysis are present in plasma
trypsin
77
enzyme activties in serum are due to
mixtures of immunologically distinct isoenzymes
78
enzymes can be used as
reagents
79
used for uric acid determination
uricase (urate oxidase)
80
In glucose determination, this enzyme reaction converts sugar other than glucose to their 6 phosphate esters
Hexokinase reaction
81
In glucose determination, this is used to monitor the change in reaction (catalyzed by G6PD)
Indicator reaction
82
equilibrium methods are also called
End point methods
83
Enzymes with high affinities for their substrate
* have low Km values * most suitable for equilibrium analysis
84
general property of first order reaction
change in substrate concentration over a fixed time interval is directly proportional to its ratio of concentration
85
most accurate for enzymatic determination of substrates; more demanding than equilibrium methods
two-point kinetic methods
86
example of enzyme labels
ALP, Horeradish, peroxidase, G6PD, B-galactosidase
87
ENZYME-LABELED ANTIBODIES OR ANTIGENS
1. react with ligand 2. enzyme substrate is added 3. washing then 2nd enzyme-labeled antibody is added 4. Ag-Ab-enzyme complex is formed 5. 2nd washing then substrate is added
88
conversion of susbtrate is proportional to
quantity of antigen
89
example of adsorbents | where immobilized enzymes are chemically bonded to
Microcrystalline cellulose, Diethylaminothyl (DEAE) cellulose, Carboxymethyl cellulose, Agarose
90
enzyme electrodes | enzymes incorporated into membranes
Ion-sensitive electrodes
91
when immersed in a solution of appropriate substrate, action of enzymes
produces ions to which electrode is sensitive

CLINICAL CHEMISTRY 2 (2 decks)

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